› 5agc

X-ray diffraction
4Å resolution

Crystallographic forms of the Vps75 tetramer

Released:
DOI: 10.2210/pdb5agc/pdb
Model geometry
Fit model/data
PDB entry 5agc coloured by chain, front view.
PDB entry 5agc coloured by chain, side view.
PDB entry 5agc coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.
Hammond CM, Sundaramoorthy R, Larance M, Lamond A, Stevens MA, El-Mkami H, Norman DG, Owen-Hughes T
OpenAccess logo Nucleic Acids Res 44 6157-72 (2016)
PMID: 27036862

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156893 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar protein sorting-associated protein 75 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 264 amino acids
Theoretical weight: 30.66 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53853 (Residues: 1-264; Coverage: 100%)
Gene names: N0890, VPS75, YNL246W
Sequence domains: Nucleosome assembly protein (NAP)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 82.75Å b: 92.43Å c: 160.75Å
α: 90° β: 93.85° γ: 90°
R-values:
R R work R free
0.231 0.229 0.265
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.
Warren et al. (2017)
2 more

4 mentions without citation

Histone chaperone networks shaping chromatin function.
Hammond et al. (2017)
3 more